FEBS Letters
Volume 583, Issue 12 , Pages 1887-1894, 18 June 2009

Maize AKINβγ dimerizes through the KIS/CBM domain and assembles into SnRK1 complexes

Edited by Gianni Cesareni

Department of Molecular Genetics, Centre de Recerca en Agrigenomica (CRAG), CSIC-IRTA-UAB, Jordi Girona 18, 08034 Barcelona, Spain

Received 5 March 2009; received in revised form 17 April 2009; accepted 6 May 2009. published online 18 May 2009.

Abstract 

The SNF1/AMPK/SnRK1 complex is an intracellular energy sensor composed of three types of subunits: the SnRK1 kinase and two regulatory, non-catalytic subunits (designated β and γ). We have previously described an atypical plant γ-subunit, AKINβγ, which contains an N-terminal tail similar to the so-called KIS domain normally present in β-subunits. However, it is not known whether AKINβγ normally associates with endogenous SnRK1 complexes in vivo, nor how its unique domain structure might contribute to SnRK1 function. Here, we present evidence that maize AKINβγ is an integral component of active SnRK1 complexes in plant cells. Using complementary methodological approaches, we also show that AKINβγ associates through homomeric interactions mediated by both, the γ- and, unexpectedly, the KIS/CBM domain.

Structured summary

MINT-7040005: AKIN (uniprotkb:B4FX20) and AKIN (uniprotkb:B4FX20) physically interact (MI:0914) by chromatography technologies (MI:0091)

MINT-7039992: AKIN (uniprotkb:B4FX20) and AKIN (uniprotkb:B4FX20) physically interact (MI:0915) by bimolecular fluorescence complementation (MI:0809)

MINT-7040024, MINT-7040044, MINT-7040067: AKIN (uniprotkb:B4FX20) and AKIN (uniprotkb:B4FX20) bind (MI:0407) by pull down (MI:0096)

MINT-7039978: SnRK1 (uniprotkb:Q8H1L5) and AKIN (uniprotkb:B4FX20) physically interact (MI:0915) by bimolecular fluorescence complementation (MI:0809)

Keywords: AKINβγ subunit, SnRK1 complex, Dimerization, KIS/CBM domain

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PII: S0014-5793(09)00384-6

doi:10.1016/j.febslet.2009.05.022

FEBS Letters
Volume 583, Issue 12 , Pages 1887-1894, 18 June 2009

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